Bacon, Kaitlyn et al. published their research in ACS Combinatorial Science in 2020 |CAS: 79642-50-5

The Article related to cyclized peptide binder yeast surface display, affinity ligands, cyclic peptides, interleukin-17 (il-17), library screening, yeast-display libraries, Biochemical Methods: Other (Not Covered At Other Subsections) and other aspects.Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate

On October 12, 2020, Bacon, Kaitlyn; Blain, Abigail; Burroughs, Matthew; McArthrur, Nikki; Rao, Balaji M.; Menegatti, Stefano published an article.Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate The title of the article was Isolation of Chemically Cyclized Peptide Binders Using Yeast Surface Display. And the article contained the following:

Cyclic peptides with engineered protein-binding activity have gained increasing attention for use in therapeutic and biotechnol. applications. The authors describe the efficient isolation and characterization of cyclic peptide binders from genetically encoded combinatorial libraries using yeast surface display. Here, peptide cyclization is achieved by disuccinimidyl glutarate-mediated crosslinking of amine groups within a linear peptide sequence that is expressed as a yeast cell surface fusion. Using this approach, the authors first screened a library of cyclic heptapeptides using magnetic selection, followed by fluorescence activated cell sorting (FACS) to isolate binders for a model target (lysozyme) with low micromolar binding affinity (KD ~1.2-3.7μM). The isolated peptides bind lysozyme selectively and only when cyclized. Importantly, yeast surface displayed cyclic peptides can be used to efficiently obtain quant. estimates of binding affinity, circumventing the need for chem. synthesis of the selected peptides. Subsequently, to demonstrate broader applicability of the authors’ approach, the authors isolated cyclic heptapeptides that bind human interleukin-17 (IL-17) using yeast-displayed IL-17 as a target for magnetic selection, followed by FACS using recombinant IL-17. Mol. docking simulations and follow-up exptl. analyses identified a candidate cyclic peptide that likely binds IL-17 in its receptor binding region with moderate apparent affinity (KD ~300 nM). Taken together, the authors’ results show that yeast surface display can be used to efficiently isolate and characterize cyclic peptides generated by chem. modification from combinatorial libraries. The experimental process involved the reaction of Bis(2,5-dioxopyrrolidin-1-yl) glutarate(cas: 79642-50-5).Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate

The Article related to cyclized peptide binder yeast surface display, affinity ligands, cyclic peptides, interleukin-17 (il-17), library screening, yeast-display libraries, Biochemical Methods: Other (Not Covered At Other Subsections) and other aspects.Name: Bis(2,5-dioxopyrrolidin-1-yl) glutarate

Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics